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Clinical Chemistry 17: 745-750, 1971;
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Clinical Chemistry, Vol 17, 745-750, Copyright © 1971 by the American Association for Clinical Chemistry

Determination of Proteins in Biological Fluids by Electroimmunodiffusion and Two-Directional Immunoelectrophoresis

Vidmantas A. Raisys 1 and Dean A. Arvan 1

1 William Pepper Laboratory, Department of Pathology, University of Pennsylvania, School of Medicine, Philadelphia, Pa. 19104.

We have used electroimmunodiffusion and two-directional immunoelectrophoresis to measure proteins in biological fluids. Electroimmunodiffusion is based on the electrophoresis of antigens in antibody-containing agarose under standardized conditions. Pre-albumin, albumin, agr1antitrypsin, agr2-macroglobulin, IgG, IgA, IgM, IgD, and other proteins have been determined in our laboratory with a precision of ±5%. The lower limit for quantitation is 5 µg/ml. For immunoglobulin quantitation, treatment of the samples with potassium cyanate (carbamylation) before electrophoresis improves sensitivity and accuracy. Two-directional immunoelectrophoresis is based on electrophoretic separation of proteins in agarose or other high-resolution media followed by electrophoresis at right angles to the first direction, in a gel in which an appropriate antiserum has been incorporated. Qualitative and semiquantitative changes in proteins in abnormal specimens can be assessed. The two techniques combined provide a very sensitive tool for the evaluation of protein changes in biologic fluids. A simple apparatus has been designed in which a number of specimens can be analyzed simultaneously by either method.


Key Words: serum, urine, cerebrospinal fluid • agarose-gel electrophoresis • carbamylation of proteins • changes in protein in disease • genetic variants of proteins






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Copyright © 1971 by the American Association for Clinical Chemistry.